Results 161 to 170 of about 8,111 (212)

Structure and cooperative formation of a FLI1 filament on contiguous GGAA DNA sites. [PDF]

Nucleic Acids Res
Hou C, Tsodikov OV.
europepmc   +1 more source

A cyclo-DOPA 6-O-glucosyltransferase-mediated route for gomphrenin I biosynthesis in Basella alba and Gomphrena globosa. [PDF]

New Phytol
Imamura T, Shigehisa R, Miyazato A, Matsumura N, Miyaki K, Segawa T, Yoshizumi M, Takagi H, Yamaguchi T, Ohki S, Mori M.   +10 more
europepmc   +1 more source

Mitigating Mn-Driven Interfacial Instability in LiMn_0.5Fe_0.5PO₄ Cathodes for Lithium-Ion Batteries via Surface-Intensive Ta Doping. [PDF]

Small
Lee H, Lee W, Jung JW, Choi W.
europepmc   +1 more source

Purification and Partial Characterization of Novel Bacteriocin L23 Produced by Lactobacillus fermentum L23

Current Microbiology, 2008
Lactobacillus fermentum strain L23 produced a small bacteriocin, designated bacteriocin L23, with an estimated molecular mass of < 7000 Da. Isolation, purification, and partial characterization of bacteriocin L23 are described. It displayed a wide inhibitory spectrum including both Gram-negative and Gram-positive pathogenic strains and two species of ...
Isabel L Barberis
exaly   +5 more sources

Inhibition of HDM2 and Activation of p53 by Ribosomal Protein L23 [PDF]

Molecular and Cellular Biology, 2004
The importance of coordinating cell growth with proliferation has been recognized for a long time. The molecular basis of this relationship, however, is poorly understood. Here we show that the ribosomal protein L23 interacts with HDM2. The interaction involves the central acidic domain of HDM2 and an N-terminal domain of L23. L23 and L11, another HDM2-
Koji Itahana, Yanping Zhang, Aiwen Jin
exaly   +5 more sources

L23 Protein Functions as a Chaperone Docking Site on the Ribosome [PDF]

Nature, 2002
During translation, the first encounter of nascent polypeptides is with the ribosome-associated chaperones that assist the folding process--a principle that seems to be conserved in evolution. In Escherichia coli, the ribosome-bound Trigger Factor chaperones the folding of cytosolic proteins by interacting with nascent polypeptides.
Günter Kramer, Holger Patzelt, Nenad Ban   +2 more
exaly   +6 more sources

NMR Structure of the Ribosomal Protein L23 From Thermus thermophilus

Journal of Biomolecular NMR, 2003
The ribosomal protein L23 is a component of the large ribosomal subunit in which it is located close to the peptide exit tunnel. In this position L23 plays a central role both for protein secretion and folding. We have determined the solution structure of L23 from Thermus thermophilus.
Torleif Härd, Maria Garber, Anders Öhman   +2 more
exaly   +4 more sources

Disruption of the MRP-L23 Gene Encoding the Mitochondrial Ribosomal Protein L23 Is Lethal for Kluyveromyces lactis but Not for Saccharomyces cerevisiae

Current Genetics, 2000
The Kluyveromyces lactis nuclear gene, MRP-L23, encodes a polypeptide of 155 amino acids that shares 70% and 43% identity to the ribosomal proteins L23 and L13 of Saccharomyces cerevisiae and Escherichia coli. The deduced protein, designated K1L23, is a likely component of the large subunit of mitochondrial ribosomes as it can complement the ...
Xin Jie Chen, Gerald L Murray, H Fukuhara   +2 more
exaly   +3 more sources